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Chloroplast localization of Cry1Ac and Cry2A protein- an alternative way of insect control in cotton Biol. Res.
Muzaffar,Adnan; Kiani,Sarfraz; Khan,Muhammad Azmat Ullah; Rao,Abdul Qayyum; Ali,Arfan; Awan,Mudassar Fareed; Iqbal,Adnan; Nasir,Idrees Ahmad; Shahid,Ahmad Ali; Husnain,Tayyab.
BACKGROUND: Insects have developed resistance against Bt-transgenic plants. A multi-barrier defense system to weaken their resistance development is now necessary. One such approach is to use fusion protein genes to increase resistance in plants by introducing more Bt genes in combination. The locating the target protein at the point of insect attack will be more effective. It will not mean that the non-green parts of the plants are free of toxic proteins, but it will inflict more damage on the insects because they are at maximum activity in the green parts of plants. RESULTS: Successful cloning was achieved by the amplification of Cry2A, Cry1Ac, and a transit peptide. The appropriate polymerase chain reaction amplification and digested products confirmed...
Tipo: Journal article Palavras-chave: Chloroplast transient peptide; Cry1Ac; Cry2A; Bt; CTP; Cry genes; Endotoxins; GUS; Transgenic plants.
Ano: 2015 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602015000100014
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Improved antifungal activity of barley derived chitinase I gene that overexpress a 32 kDa recombinant chitinase in Escherichia coli host BJM
Toufiq,Nida; Tabassum,Bushra; Bhatti,Muhammad Umar; Khan,Anwar; Tariq,Muhammad; Shahid,Naila; Nasir,Idrees Ahmad; Husnain,Tayyab.
Abstract Agricultural crops suffer many diseases, including fungal and bacterial infections, causing significant yield losses. The identification and characterisation of pathogenesis-related protein genes, such as chitinases, can lead to reduction in pathogen growth, thereby increasing tolerance against fungal pathogens. In the present study, the chitinase I gene was isolated from the genomic DNA of Barley (Hordeum vulgare L.) cultivar, Haider-93. The isolated DNA was used as template for the amplification of the ∼935 bp full-length chitinase I gene. Based on the sequence of the amplified gene fragment, class I barley chitinase shares 93% amino acid sequence homology with class II wheat chitinase. Interestingly, barley class I chitinase and class II...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Antifungal activity assay; Barley chitinase class I; Escherichia coli expression; Recombinant chitinase protein.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822018000200414
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